6AR1

Structure of a Thermostable Group II Intron Reverse Transcriptase with Template-Primer and Its Functional and Evolutionary Implications (RT/Duplex (Nat))

Summary for 6AR1

• Entry DOI: 10.2210/pdb6ar1/pdb
• Related: 6AR3 6AR5
• Descriptor: GsI-IIC RT, DNA, RNA, ... (6 entities in total)
• Functional Keywords: polymerase, rna binding protein-rna-dna complex, rna binding protein/rna/dna
• Biological source: Geobacillus stearothermophilus (Bacillus stearothermophilus); More
• Total number of polymer chains: 6
• Total formula weight: 116356.13

Authors

Stamos, J.L.,Lentzsch, A.M.,Lambowitz, A.M. (deposition date: 2017-08-21, release date: 2017-11-29, Last modification date: 2023-10-04)

Primary citation

Stamos, J.L.,Lentzsch, A.M.,Lambowitz, A.M.
Structure of a Thermostable Group II Intron Reverse Transcriptase with Template-Primer and Its Functional and Evolutionary Implications.
Mol. Cell, 68:926-939.e4, 2017

PubMed Abstract: Bacterial group II intron reverse transcriptases (RTs) function in both intron mobility and RNA splicing and are evolutionary predecessors of retrotransposon, telomerase, and retroviral RTs as well as the spliceosomal protein Prp8 in eukaryotes. Here we determined a crystal structure of a full-length thermostable group II intron RT in complex with an RNA template-DNA primer duplex and incoming deoxynucleotide triphosphate (dNTP) at 3.0-Å resolution. We find that the binding of template-primer and key aspects of the RT active site are surprisingly different from retroviral RTs but remarkably similar to viral RNA-dependent RNA polymerases. The structure reveals a host of features not seen previously in RTs that may contribute to distinctive biochemical properties of group II intron RTs, and it provides a prototype for many related bacterial and eukaryotic non-LTR retroelement RTs. It also reveals how protein structural features used for reverse transcription evolved to promote the splicing of both group II and spliceosomal introns.

PubMed: 29153391
DOI: 10.1016/j.molcel.2017.10.024

Experimental method

X-RAY DIFFRACTION (3.01 Å)